Abstract:Xuanen ham processing was divided into five stages，and changes in protein interactions at each stage were determined and analyzed.Interactions were mediated primarily by hydrophobic effects and ionic bonds in the raw leg.Interactions in finished hams were largely mediated by hydrophobic effects and disulfide bonds.During processing，the relative content of ionic and hydrogen bonds decreases，while the relative content of hydrophobic interactions and disulfide bonds increases.From the raw leg to the finished ham，the bromophenol blue binding myofibrillar protein content increased from 9.09 μg to 38.7 μg.The increase in surface hydrophobicity may be related to protein oxidation.The carbonyl content（characteristic of the degree of protein oxidation）increased from 0.68 nmol/mg in the raw leg，to 2.28 nmol/mg in the finished ham.This trend was consistent with the observed change in surface hydrophobicity.During the processing of Xuanen ham，sulfhydryl groups were oxidized upon exposure，forming disulfide bonds.Disulfide bond content increased from 9.65 nmol/mg in the raw leg，to 21.6 nmol/mg in finished ham.Surface hydrophobicity and disulfide bonds were important forces that stabilize protein tertiary structures.Enrichment in these forces contributes to the stability of Xuanen ham structure and function during its long fermentation period.